Saliva contains a broad spectrum of proteins which are known to play an important role in maintaining the integrity of the hard and soft oral tissues. Many of the proteins secreted from the parotid glands are glycoproteins and have their oligosaccharides attached to asparagine residues, so-called N-linked glycoproteins. To study the mechanisms envolved in processing, synthesis and secretion of N-linked secretory proteins, we have utilized in vitro cell preparations from rat parotid glands. We ahve shown that the potent Beta-adrenergic agonist (-)-isoproterenol increases (3H) mannose incorporation into newly synthesized glycoproteins. This effect in the rat parotid acinar cells is mediated by cyclic AMP. During the present reporting period, we have investigated (1) the synthesis of mannosylphosphoryl-dolichol, oligosaccharide-PP-dolichol and the turn over of the oligosaccharide-PP-dolichol pool after Beta-adrenoreceptor stimulation; (2) the regulation of several "key" enzymatic steps in protein N-glycosylation which may be reasonable sites for the observed enhancement of protein glycosylation seen after (-)-isoproterenol treatment and (3) Beta-adrenoreceptor effects on oligosaccharide processing.